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Reviewed, UniProtKB/Swiss-Prot P56961 (ARODE_CHLMU)

Last modified February 9, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Shikimate biosynthesis protein aroDE
Including the following 2 domains:
    1- Recommended name:
            3-dehydroquinate dehydratase
                Short name=3-dehydroquinase
              EC=4.2.1.10
        Alternative name(s):
            Type I DHQase
    2- Recommended name:
            Shikimate dehydrogenase
              EC=1.1.1.25
Gene names
Name: aroE
Synonyms: aroD/E
Ordered Locus Names: TC_0649
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes two sequential steps of the aromatic amino acids biosynthetic pathway. The first reaction is catalyzed by the 3-dehydroquinate dehydratase, coded by the aroD domain; the second reaction is catalyzed by the shikimate 5-dehydrogenase, coded by the aroE domain. HAMAP MF_00214

Catalytic activity

3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP MF_00214

Shikimate + NADP+ = 3-dehydroshikimate + NADPH. HAMAP MF_00214

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP MF_00214

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.

Sequence similarities

In the N-terminal section; belongs to the type-I 3-dehydroquinase family.

In the C-terminal section; belongs to the shikimate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478Shikimate biosynthesis protein aroDE HAMAP MF_00214
PRO_0000138822

Regions

Nucleotide binding337 – 3415NADP By similarity
Region1 – 2082083-dehydroquinate dehydratase HAMAP MF_00214
Region209 – 478270Shikimate 5-dehydrogenase HAMAP MF_00214

Sites

Active site1101Proton acceptor By similarity
Active site1331Schiff-base intermediate with substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P56961-1 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 199EEF5251205AB9

FASTA47853,211
        10         20         30         40         50         60 
MLCTIIRGPS FLEARNQLLR SLKKCRCFEM RADLLTVSDA ELQKLILLAP ISVLTWKKPP 

        70         80         90        100        110        120 
SCTPQAWVKK IQSLAKLHPT YLDLDKDFPE EEILHIRHLH PNIKIIRSLH TSEHTDITQL 

       130        140        150        160        170        180 
YTQMLASSID YYKLAVSPAS TTDLLNICRQ KHSLPQNTTV LCLGKIGQSS RILSPILQNP 

       190        200        210        220        230        240 
FTYTIPTGAD PVAPGQLSLN HHYFYNFTNL SPQSQICALI GDTSRSIGHL THNPFFSQLS 

       250        260        270        280        290        300 
IPCPYVKLPL TPQELPEFFS SIRALPFLGI SVTSPLKTAI IPFLDKQDSS VKLSGSCNTL 

       310        320        330        340        350        360 
VIRQGEIIGY DTDGEGLFSV LTQHNMDLSN QRVAILGAGG AARSIAARLS RTGCELLIFN 

       370        380        390        400        410        420 
RTKIHAEAIA SRYQAQAFDI KDLPLHSVSL IINCLPPSSI IPQALAPLIV DINTLPKHNS 

       430        440        450        460        470 
FTQYARLKGC SIIYGHEMFA QQALLQFRLW FPTHSFNHLE KNFSRRAAVL ASLFSIAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39475.1.
PIRG81679.
RefSeqNP_297023.1.

3D structure databases

SMRP56961. Positions 1-453.
ModBaseSearch...

Genome annotation databases

GeneID1246010.
GenomeReviewsGene locus TC_0649 in contig AE002160_GR.
KEGGcmu:TC0649.
TIGRTC_0649.

Phylogenomic databases

HOGENOMHBG414053.
OMAISHLSHN.

Enzyme and pathway databases

BioCycCMUR243161:TC_0649-MONOMER.
BRENDA1.1.1.25. 256349.
4.2.1.10. 256349.

Family and domain databases

HAMAPMF_00214. AroD. Fused.
[Tree]
MF_00222. Shikimate_DH_AroE. Fused.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
IPR016040. NAD(P)-bd_dom.
IPR011342. Quinate/shikimate_5-DH.
IPR013708. Shikimate_DH-bd_N.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01487. DHquinase_I. 1 hit.
PF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00507. aroE. 1 hit.
PROSITEPS01028. DEHYDROQUINASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARODE_CHLMU
AccessionPrimary (citable) accession number: P56961
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents